LOCUS       NM_001013853             545 bp    mRNA    linear   ROD 28-MAR-2024
DEFINITION  Rattus norvegicus hemoglobin alpha, adult chain 3 (Hba-a3), mRNA.
ACCESSION   NM_001013853 XM_347150
VERSION     NM_001013853.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (bases 1 to 545)
  AUTHORS   Marcos-Almaraz,M.T., Rodriguez-Gomez,J.A., Lopez-Barneo,J. and
            Pascual,A.
  TITLE     alpha-Haemoglobin regulates sympathoadrenal cell metabolism to
            maintain a catecholaminergic phenotype
  JOURNAL   Biochem J 441 (3), 843-850 (2012)
   PUBMED   22060312
  REMARK    GeneRIF: A role for alpha-haemoglobin is a regulator of
            catecholaminergic cell metabolism required for phenotype
            acquisition and maintenance.
REFERENCE   2  (bases 1 to 545)
  AUTHORS   Fornander,L., Ghafouri,B., Kihlstrom,E., Akerlind,B., Schon,T.,
            Tagesson,C. and Lindahl,M.
  TITLE     Innate immunity proteins and a new truncated form of SPLUNC1 in
            nasopharyngeal aspirates from infants with respiratory syncytial
            virus infection
  JOURNAL   Proteomics Clin Appl 5 (9-10), 513-522 (2011)
   PUBMED   21805676
REFERENCE   3  (bases 1 to 545)
  AUTHORS   Kapralov,A., Vlasova,I.I., Feng,W., Maeda,A., Walson,K.,
            Tyurin,V.A., Huang,Z., Aneja,R.K., Carcillo,J., Bayir,H. and
            Kagan,V.E.
  TITLE     Peroxidase activity of hemoglobin-haptoglobin complexes: covalent
            aggregation and oxidative stress in plasma and macrophages
  JOURNAL   J Biol Chem 284 (44), 30395-30407 (2009)
   PUBMED   19740759
REFERENCE   4  (bases 1 to 545)
  AUTHORS   Deng,L., Pan,X., Wang,Y., Wang,L., Zhou,X.E., Li,M., Feng,Y.,
            Wu,Q., Wang,B. and Huang,N.
  TITLE     Hemoglobin and its derived peptides may play a role in the
            antibacterial mechanism of the vagina
  JOURNAL   Hum Reprod 24 (1), 211-218 (2009)
   PUBMED   18786935
REFERENCE   5  (bases 1 to 545)
  AUTHORS   Storz,J.F., Hoffmann,F.G., Opazo,J.C. and Moriyama,H.
  TITLE     Adaptive functional divergence among triplicated alpha-globin genes
            in rodents
  JOURNAL   Genetics 178 (3), 1623-1638 (2008)
   PUBMED   18245844
  REMARK    GeneRIF: The objective of this study was to test whether amino acid
            differences among triplicated alpha-globin paralogs are
            attributable to a relaxation of purifying selection or to a history
            of positive selection.
REFERENCE   6  (bases 1 to 545)
  AUTHORS   Groff,P., Galacteros,F., Kalmes,G., Blouquit,Y. and Wajcman,H.
  TITLE     Hb Luxembourg [alpha 24(B5) Tyr----His]: a new unstable variant
  JOURNAL   Hemoglobin 13 (5), 429-436 (1989)
   PUBMED   2599879
REFERENCE   7  (bases 1 to 545)
  AUTHORS   Baklouti,F., Baudin-Chich,V., Kister,J., Marden,M., Teyssier,G.,
            Poyart,C., Delaunay,J. and Wajcman,H.
  TITLE     Increased oxygen affinity with normal heterotropic effects in
            hemoglobin Loire [alpha 88(F9)Ala----Ser]
  JOURNAL   Eur J Biochem 177 (2), 307-312 (1988)
   PUBMED   3142772
REFERENCE   8  (bases 1 to 545)
  AUTHORS   Ohba,Y., Yamamoto,K., Hattori,Y., Kawata,R. and Miyaji,T.
  TITLE     Hyperunstable hemoglobin Toyama [alpha 2 136(H19)Leu----Arg beta
            2]: detection and identification by in vitro biosynthesis with
            radioactive amino acids
  JOURNAL   Hemoglobin 11 (6), 539-556 (1987)
   PUBMED   2833478
REFERENCE   9  (bases 1 to 545)
  AUTHORS   John,M.E.
  TITLE     Structural, functional and conformational properties of rat
            hemoglobins
  JOURNAL   Eur J Biochem 124 (2), 305-310 (1982)
   PUBMED   6284505
REFERENCE   10 (bases 1 to 545)
  AUTHORS   Chua,C.G. and Carrell,R.W.
  TITLE     Three cysteine residues in the alpha chain of rat haemoglobin
            (albino Rattus norvegicus): 13 (A 11), 104 (G 11) and 111 (G 18)
  JOURNAL   Biochim Biophys Acta 365 (2), 328-334 (1974)
   PUBMED   4429672
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Dec 20, 2019 this sequence version replaced NM_001013853.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ212394.1, FQ224052.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676787, SAMN16676808
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-126               JAXUCZ010000010.1  15816818-15816943   c
            127-331             JAXUCZ010000010.1  15816498-15816702   c
            332-545             JAXUCZ010000010.1  15816099-15816312   c
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Rattus norvegicus"
                     /mol_type="mRNA"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     gene            1..545
                     /gene="Hba-a3"
                     /gene_synonym="Glnc1; GloA; Hba-a1"
                     /note="hemoglobin alpha, adult chain 3"
                     /db_xref="GeneID:287167"
                     /db_xref="RGD:1359209"
     exon            1..126
                     /gene="Hba-a3"
                     /gene_synonym="Glnc1; GloA; Hba-a1"
                     /inference="alignment:Splign:2.1.0"
     CDS             32..460
                     /gene="Hba-a3"
                     /gene_synonym="Glnc1; GloA; Hba-a1"
                     /note="alpha-globin; globin, alpha; globin c1; hemoglobin
                     alpha, adult chain 1"
                     /codon_start=1
                     /product="hemoglobin alpha, adult chain 3"
                     /protein_id="NP_001013875.1"
                     /db_xref="GeneID:287167"
                     /db_xref="RGD:1359209"
                     /translation="MVLSEEDKNNIKKAWVKIGNHAAEIGAETIGRLFIVFPSSKTYF
                     PHFNTSEGSDQVKAHGKKVADALTNAASHLDDLPGALSTLSDLHAHKLRVDPVNFKFL
                     SHCLLVTLASHHPGDFTPAMHASLDKFFASVSTVLTSKYR"
     exon            127..331
                     /gene="Hba-a3"
                     /gene_synonym="Glnc1; GloA; Hba-a1"
                     /inference="alignment:Splign:2.1.0"
     exon            332..545
                     /gene="Hba-a3"
                     /gene_synonym="Glnc1; GloA; Hba-a1"
                     /inference="alignment:Splign:2.1.0"
ORIGIN      
        1 attctcattc tgatagactc aggaagcaat catggtgctc tctgaagagg acaaaaacaa
       61 catcaagaaa gcctgggtga agattggtaa ccatgctgct gaaattggcg cagagaccat
      121 agggaggttg ttcattgtct tcccctcctc caagacctac ttccctcact ttaatacaag
      181 tgagggctcc gaccaggtca aggctcacgg caagaaggtt gctgatgccc tgaccaatgc
      241 tgcaagccac ctcgatgacc tgcctggtgc cctgtccact ctgagcgacc tgcatgccca
      301 caaactgcgt gtggatcctg tcaacttcaa gttcttgagc cactgcctgc tggtgacctt
      361 ggctagccac caccctgggg atttcacacc cgccatgcac gcctctctgg acaaattctt
      421 tgcctctgtg agcactgtgt tgacttccaa gtaccgttaa gccacttcct gtcggtcttg
      481 ccttctgacc aggcccttct tcactccctt gcacctgtct ttgaataaag caaaagtagg
      541 aagaa
//
